4BIN
Crystal structure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-10-01 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 59.032, 68.442, 90.576 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 90.580 - 2.490 |
| R-factor | 0.17834 |
| Rwork | 0.176 |
| R-free | 0.23101 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ne8 |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.625 |
| Data reduction software | XDS |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.500 | 2.560 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.200 | 1.000 |
| Number of reflections | 13314 | |
| <I/σ(I)> | 12.8 | 2.2 |
| Completeness [%] | 99.9 | 99.8 |
| Redundancy | 12.7 | 7.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 12 | 20% PEG 8000, 0.1 M CABS PH 12, 20 MM COCL2 |
